IndraLab

"The phosphorylation of rpS6 at S235 and S236 can be mediated by RSK and/or p70S6K."

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"A knockin mouse carrying mutations at all phosphorylation sites in the primary s6k substrate, ribosomal protein s6 (rps6), has provided insight into the physiological role of this protein phosphorylation event. Of the many known substrates of s6k1, it is rps6 that has been shown to be directly involved, via its phosphorylation, in controlling cell size."

"After stimulation, S6K1 phosphorylates S6 on five serine residues (S235, S236, S240, S244, and S247) within the C-terminus [XREF_BIBR]."

No evidence text available

"XREF_BIBR S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247."

"A recent bioinformatics study performed KEGG analysis and gene set enrichment analysis (GSEA) via Gene Expression Profiling Interactive Analysis (GEPIA) based on The Cancer Genome Atlas (TCGA) datasets and demonstrated that ACTL6A significantly affects ribosomal pathways. xref Since S6 kinase (S6K1) is a key member of the pathway, that participates in translational control, and the S6 kinase (S6K1)-S6 signaling pathway is critical for regulating proliferation and survival in response to growth factors, we focused on S6K1 as a downstream target of ACTL6A. xref S6K1 always phosphorylates S6 protein at Ser235, Ser236, Ser240, Ser244, and Ser247. xref Aberrant upregulation of S6 phosphorylation and increased S6K activity are frequently present in various tumors including ESCC. xref Although phosphorylated-ribosomal protein S6 (p-S6) is considered to be a potential target in ESCC in vitro and S6 phosphorylation has prognostic significance in ESCC, the relationship between S6 and ACTL6A remains unclear. xref "

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No evidence text available

"XREF_BIBR The S6K1 dependent regulation of cellular size is mediated by ribosomal protein S6, which is phosphorylated by S6K1 and the closely related S6K2 on Ser235 and Ser236."